[1]	NUCLEOTIDE SEQUENCE [MRNA]. PubMed=1894602 [NCBI, ExPASy, EBI, Israel, Japan] Boese Q.F., Spano A.J., Li J., Timko M.P.; "Aminolevulinic acid dehydratase in pea (Pisum sativum L.). Identification of an unusual metal-binding domain in the plant enzyme."; J. Biol. Chem. 266:17060-17066(1991).

Comments

CATALYTIC ACTIVITY: 2 5-aminolevulinate = porphobilinogen + 2 H₂O.
COFACTOR: Magnesium.
PATHWAY: Porphyrin metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen III from 5-aminolevulinate: step 1/4 .
SUBUNIT: Homooctamer (By similarity).
SUBCELLULAR LOCATION: Plastid, chloroplast.
SIMILARITY: Belongs to the ALADH family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

M71235; AAA33640.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A40966; A40966.

3D structure databases

HSSP

P13716; 1E51. [HSSP ENTRY / PDB]

ModBase

P30124.

Ontologies

GO:0009507;	Cellular component: chloroplast (inferred from electronic annotation from UniProtKB-KW).
GO:0000287;	Molecular function: magnesium ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0004655;	Molecular function: porphobilinogen synthase activity (inferred from electronic annotation from InterPro).
GO:0015995;	Biological process: chlorophyll biosynthetic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001731; 4pyrrol_synth_porphobiln_synth.
IPR013785; Aldolase_TIM.
Graphical view of domain structure.

Gene3D

G3DSA:3.20.20.70; Aldolase_TIM; 1.

PANTHER

PTHR11458; AlaD_dehydratase; 1.

Pfam

PF00490; ALAD; 1.
Pfam graphical view of domain structure.

PRINTS

PR00144; DALDHYDRTASE.

ProDom

PD002304; AlaD_dehydratase; 1.
[Domain structure / List of seq. sharing at least 1 domain]

PROSITE

PS00169; D_ALA_DEHYDRATASE; 1.

Other

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Chlorophyll biosynthesis; Chloroplast; Lyase; Magnesium; Plastid; Porphyrin biosynthesis; Transit peptide.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`TRANSIT`	`<1 ?`		`Chloroplast.`
`CHAIN`	`? 398`		`Delta-aminolevulinic acid dehydratase, chloroplastic.`	`PRO_0000013317`
`REGION`	`187 205`	`19`	`Magnesium-binding (By similarity).`
`ACT_SITE`	`319 319`		`By similarity.`
`NON_TER`	`1 1`

Sequence information

Length: 398 AA [This is the length of the partial sequence of the unprocessed precursor]

Molecular weight: 43815 Da [This is the MW of the partial sequence of the unprocessed precursor]

CRC64: 75DDCB55CE3C6BD1 [This is a checksum on the sequence]

        10         20         30         40         50         60 
HTFVDLKSPF TLSNYLSFSS SKRRQPPSLF TVRASDSDFE AAVVAGKVPE APPVPPTPAS 

        70         80         90        100        110        120 
PAGTPVVPSL PIQRRPRRNR RSPALRSAFQ ETTLSPANFV YPLFIHEGEE DTPIGAMPGC 

       130        140        150        160        170        180 
YRLGWRHGLL EEVAKARDVG VNSVVLFPKI PDALKTPTGD EAYNEDGLVP RSIRLLKDKY 

       190        200        210        220        230        240 
PDLIIYTDVA LDPYSSDGHD GIVREDGVIM NDETVHQLCK QAVAQARAGA DVVSPSDMMD 

       250        260        270        280        290        300 
GRVGAMRVAL DAEGFQHVSI MSYTAKYASS FYGPFREALD SNPRFGDKKT YQMNPANYRE 

       310        320        330        340        350        360 
ALTEMREDES EGADILLVKP GLPYLDIIRL LRDNSPLPIA AYQVSGEYSM IKAGGALKMI 

       370        380        390 
DEEKVMMESL LCLRRAGADI ILTYFALQAA RTLCGEKR

P30124 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools